STANFORD

UNIVERSITY

---- A team of investigators led by Stanford University researchers have discovered the cause and a potential treatment for celiac sprue, an autoimmune disease that leads to an inability to digest gluten, a major protein in wheat, rye and barley products. The disease is estimated to afflict as many as 1 in 200 Americans. In the Sept. 27 issue of Science, researchers identify a fragment of gluten called gliadin as the celiac culprit. They showed that this fragment is resistant to digestion and is responsible for the intestine-damaging inflammatory response experienced by celiac patients. They also report the use of a dietary enzyme made by a bacterium that can break down the fragment into harmless bits, suggesting future treatment through dietary supplements.

“The only effective therapy for most people is a lifelong gluten-free diet, and that’s fairly restrictive,” explained co-author Gary M. Gray, professor of medicine, emeritus. The diet is essential over the long term both to restore normal intestinal function and to reduce the risk of developing osteoporosis, lymphoma or cancer of the small intestine, he added.

In the laboratory, Shan simulated the digestive process, exposing gliadin to digestive enzymes in test tubes. She identified a protein fragment made up of a 33 amino acids that was resistant to further digestion between two and six amino acids or into single amino acids. She then repeated her study in rats and again in test tubes using tissue taken by biopsy from patients undergoing unrelated medical procedures. “Even with prolonged treatment (exposure to intestinal enzymes), the peptide doesn’t lose the ability to induce the inflammatory response,” Shan said.

When they looked more closely at the fragment, Shan and her colleagues found that it was made up of even smaller fragments already known to induce human Because the fragment is rich in the amino acid proline, investigators reasoned that a peptidase (an enzyme that breaks down proteins) with the ability to digest proline-rich chains might be able to break down the gliadin fragment, rendering it harmless to celiac patients. They have now shown that this is the case in test tubes and in rats. Because there are no animal models of celiac disease, testing this approach in humans is a long way off and will require further preclinical work, Khosla said. “We think that this mode of therapy – peptidase supplementation – may offer hope in treating celiac sprue eventually, and we’re going to test this hypothesis.”

This research was very exciting for us at Neutraceutical Formularies and we used this study and others to make sure LactoGlutenZyme has the exact peptidase enzyme combination and strength to digest gluten proteins. The research is very specific toward the pH levels and precursors needed to ensure the complete breakdown and elimination of Gluten peptides.

Although, there is no cure for serious gluten intolerant concerns like celiac disease, we are excited to help those with gluten sensitivities and others that are worried about digesting hidden glutens and other proteins within their diet.

Because LactoGlutenZyme is so packed with protein digesting power, this formula works great with Paleo diets and other high protein eating plans.

NOTE; If you do have celiac disease or any other medical condition, it is imperative that you consult with your physician and show the research to him/her before changing your prescribed program. Many physicians are excited about helping their patients better digest the hidden proteins in diets that might cause intestinal and extra-intestinal discomfort and stunted growth typical to starvation.